HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Brauker, J. H. Articles by Wang, J. L. Search for Related Content PubMed PubMed Citation Articles by Brauker, J. H. Articles by Wang, J. L. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 262, Issue 27, 13093-13101, Sep, 1987

Nonlysosomal processing of cell-surface heparan sulfate proteoglycans. Studies of I-cells and NH4Cl-treated normal cells

JH Brauker and JL Wang
Department of Biochemistry, Michigan State University, East Lansing 48824.

The metabolism of cell-associated proteoglycans, labeled in the glycosaminoglycan portion with 35SO2-4, was studied in normal skin fibroblasts (SL66 cells), NH4Cl-treated SL66 fibroblasts, and in I- cells derived from patients with mucolipidosis II. Kinetic data from label-chase experiments and gel filtration analysis of the molecular weight distribution of the radiolabeled glycosaminoglycans indicated that I-cells and NH4Cl-treated normal fibroblasts (a) internalize cell surface proteoglycans, (b) remove glycosaminoglycan chains from proteoglycan core proteins, and (c) degrade heparan sulfate glycosaminoglycan chains via an endoglycosidic activity. These processes occur with rates comparable to those in normal fibroblasts. The data are consistent with the hypothesis that the glycosaminoglycan chains of cell-surface proteoglycans are separated from the protein cores in a nonlysosomal compartment prior to the transport of these chains to lysosomes for degradation. These observations also raise the possibility that this early step in separation of glycosaminoglycan chains from protein cores may serve to regulate the levels of glycosaminoglycan-free core protein observed in various cells.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				K. J. Bame Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans Glycobiology, June 1, 2001; 11(6): 91R - 98R. [Abstract] [Full Text] [PDF]

				K. J. Bame, J. Danda, A. Hassall, and S. Tumova Abeta (1-40) Prevents Heparanase-catalyzed Degradation of Heparan Sulfate Glycosaminoglycans and Proteoglycans in Vitro. A ROLE FOR HEPARAN SULFATE PROTEOGLYCAN TURNOVER IN ALZHEIMER'S DISEASE J. Biol. Chem., July 4, 1997; 272(27): 17005 - 17011. [Abstract] [Full Text] [PDF]

				S. Tumova and K. J. Bame The Interaction between Basic Fibroblast Growth Factor and Heparan Sulfate Can Prevent the in Vitro Degradation of the Glycosaminoglycan by Chinese Hamster Ovary Cell Heparanases J. Biol. Chem., April 4, 1997; 272(14): 9078 - 9085. [Abstract] [Full Text] [PDF]